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I3382

Sigma-Aldrich

Anti-Human IgG (γ-chain specific) antibody produced in goat

affinity isolated antibody, lyophilized powder

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

lyophilized powder

technique(s)

Ouchterlony double diffusion: suitable

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

IgG antibody subtype is the most abundant serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defence of the neonate against infections. Anti-Human IgG (γ-chain specific) antibody is specific for γ chain of all human IgG subclasses.
Immunoglobulins (Igs) belong to the immunoglobulin super-family and have two heavy (H) and two light (L) chains, held together by disulphide linkages. The L chain comprises of one variable N-terminal region and a constant C-terminal region. The heavy chain has one variable N-terminal region and three to four constant (CH1-CH4) C-terminal regions. IgG is an abundant protein in human serum. The four classes of IgG include IgG1, IgG2, IgG3 and IgG4. The IgG heavy chain region is mapped to human chromosome 14.

Immunogen

Purified human IgG

Application

Anti-Human IgG (γ-chain specific) antibody was used as a standard in ELISA and radioimmunoassay.

Biochem/physiol Actions

IgG1 class is the most abundant and its deficiency results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions and IgG4 is associated with asymptomatic infection. Digestion of IgG by papain results in generation of fragment antigen binding (Fab). Pepsin digestion of IgG results in fragment crystallizable (Fc). The Fc region of IgG antibody has enormous therapeutic potential and is exploited for the development of therapeutic antibodies.

Physical form

Lyophilized from 0.01 M sodium phosphate, 0.015 M sodium chloride, pH 7.2

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Andreas Maccani et al.
Applied microbiology and biotechnology, 98(17), 7535-7548 (2014-07-24)
MicroRNAs are short non-coding RNAs that play an important role in the regulation of gene expression. Hence, microRNAs are considered as potential targets for engineering of Chinese hamster ovary (CHO) cells to improve recombinant protein production. Here, we analyzed and
R J Cox et al.
APMIS : acta pathologica, microbiologica, et immunologica Scandinavica, 107(3), 289-296 (1999-05-01)
The radio-immunoblot (RIB) assay was used to examine the antibody response to proteins of the vaccine strains induced after influenza vaccination. Vaccination stimulated an antibody response to the surface glycoproteins (HA and NA) and to the internal antigens (NP and
Juan A Hernández Bort et al.
Biotechnology journal, 5(10), 1090-1097 (2010-10-12)
During the process of recombinant cell line optimisation for production of biopharmaceuticals, multiple cellular properties like robustness against stress, the attainment of high cell concentrations and maintenance of high viability must be considered to maximize protein yield. To improve growth
Wolfgang Sommeregger et al.
Biotechnology and bioengineering, 113(9), 1902-1912 (2016-02-26)
Chinese hamster ovary (CHO) cells are the most commonly used mammalian hosts for the production of biopharmaceuticals. To overcome unfavorable features of CHO cells, a lot of effort is put into cell engineering to improve phenotype. "Omics" studies investigating elevated
Andreas Maccani et al.
Biotechnology journal, 9(4), 526-537 (2014-01-07)
Chinese hamster ovary (CHO) cells are currently the workhorse of the biopharmaceutical industry. However, yeasts such as Pichia pastoris are about to enter this field. To compare their capability for recombinant protein secretion, P. pastoris strains and CHO cell lines

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